scholarly journals Characterization of a U.S. Isolate of Beet black scorch virus

2007 ◽  
Vol 97 (10) ◽  
pp. 1245-1254 ◽  
Author(s):  
John J. Weiland ◽  
David Van Winkle ◽  
Michael C. Edwards ◽  
Rebecca L. Larson ◽  
Weilin L. Shelver ◽  
...  
Keyword(s):  
Coat Protein ◽  
Protein Gene ◽  
Sequence Similarity ◽  
Systemic Infection ◽  
Amino Acid Sequence Similarity ◽  
Adenosine Nucleotides ◽  
Tetragonia Expansa ◽  
Extension Analysis ◽  
Beet Black Scorch Virus

The first reported U.S. isolate of Beet black scorch necrovirus (BBSV) was obtained and characterized. Host range of the virus for localized and occasionally systemic infection included the Chenopodiaceae and Tetragonia expansa; Nicotiana benthamiana supported symptomless systemic infection by the virus. The complete nucleotide sequence of the genomic RNA of the virus, designated BBSV-Co, exhibits 93% similarity to the genome of the ‘Ningxia’ isolate of BBSV from China. Amino acid sequence similarity in predicted genes ranged from 95% in the p4 gene to 97% in the p82 and coat protein genes. A potential additional gene exists within the U.S. isolate of BBSV that is absent from Chinese isolates of BBSV due to nucleotide differences between these isolates within the coat protein gene. Coat protein analysis by isoelectric focusing and by mass spectroscopy indicated the presence of phosphorylated residues. Using primer extension analysis of the 5′ end of the genome and site-directed mutants of genomic clones of BBSV-Co from which infectious RNA was produced, the native 5′ end of the BBSV-Co genome was determined to be 5′-GAAACCTAACC…3′, lacking the two terminal adenosine nucleotides in the published sequences of BBSV from China.

Molecular detection and coat protein gene based characterization of Citrus tristeza virus prevalent in Sikkim state of India

2019 ◽  
Vol 73 (1) ◽  
pp. 135-143 ◽  
Author(s):  
Ashish Warghane ◽  
Amol Kokane ◽  
Sunil Kokane ◽  
Manali Motghare ◽  
Datta Surwase ◽  
...  
Keyword(s):  
Coat Protein ◽  
Coat Protein Gene ◽  
Molecular Detection ◽  
Citrus Tristeza Virus ◽  
Protein Gene ◽  
Tristeza Virus ◽  
Citrus Tristeza

scholarly journals Engineered Resistance Against Papaya ringspot virus in Venezuelan Transgenic Papayas

Plant Disease ◽  
2004 ◽  
Vol 88 (5) ◽  
pp. 516-522 ◽  
Author(s):  
Gustavo Fermin ◽  
Valentina Inglessis ◽  
Cesar Garboza ◽  
Sairo Rangel ◽  
Manuel Dagert ◽  
...  
Keyword(s):  
Amino Acid ◽  
Agrobacterium Tumefaciens ◽  
Coat Protein ◽  
Amino Acid Sequence ◽  
Sequence Similarity ◽  
Ringspot Virus ◽  
Amino Acid Sequence Similarity ◽  
Papaya Ringspot Virus ◽  
Local Varieties ◽  
Cp Gene

Local varieties of papaya grown in the Andean foothills of Mérida, Venezuela, were transformed independently with the coat protein (CP) gene from two different geographical Papaya ringspot virus (PRSV) isolates, designated VE and LA, via Agrobacterium tumefaciens. The CP genes of both PRSV isolates show 92 and 96% nucleotide and amino acid sequence similarity, respectively. Four PRSV-resistant R0 plants were intercrossed or selfed, and the progenies were tested for resistance against the homologous isolates VE and LA, and the heterologous isolates HA (Hawaii) and TH (Thailand) in greenhouse conditions. Resistance was affected by sequence similarity between the transgenes and the challenge viruses: resistance values were higher for plants challenged with the homologous isolates (92 to 100% similarity) than with the Hawaiian (94% similarity) and, lastly, Thailand isolates (88 to 89% similarity). Our results show that PRSV CP gene effectively protects local varieties of papaya against homologous and heterologous isolates of PRSV.

Preliminary x-ray characterization of authentic providence virus and attempts to express its coat protein gene in recombinant baculovirus

2005 ◽  
Vol 151 (1) ◽  
pp. 155-165 ◽  
Author(s):  
D. J. Taylor ◽  
J. A. Speir ◽  
V. Reddy ◽  
G. Cingolani ◽  
F. M. Pringle ◽  
...  
Keyword(s):  
Coat Protein ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Recombinant Baculovirus ◽  
X Ray

scholarly journals Characterization of the maize Mutator transposable element MURA transposase as a DNA-binding protein.

1997 ◽  
Vol 17 (9) ◽  
pp. 5165-5175 ◽  
Author(s):  
M I Benito ◽  
V Walbot
Keyword(s):  
Dna Binding ◽  
Transposable Element ◽  
Binding Protein ◽  
Sequence Similarity ◽  
Functional Characterization ◽  
Dna Binding Protein ◽  
Amino Acid Sequence Similarity ◽  
Mobility Shift ◽  
Gel Mobility Shift

The autonomous MuDR element of the Mutator (Mu) transposable element family of maize encodes at least two proteins, MURA and MURB. Based on amino acid sequence similarity, previous studies have reported that MURA is likely to be a transposase. The functional characterization of MURA has been hindered by the instability of its cDNA, mudrA, in Escherichia coli. In this study, we report the first successful stabilization and expression of MURA in Saccharomyces cerevisiae. Gel mobility shift assays demonstrate that MURA is a DNA-binding protein that specifically binds to sequences within the highly conserved Mu element terminal inverted repeats (TIRs). DNase I and 1,10-phenanthroline-copper footprinting of MURA-Mu1 TIR complexes indicate that MURA binds to a conserved approximately 32-bp region in the TIR of Mu1. In addition, MURA can bind to the same region in the TIRs of all tested actively transposing Mu elements but binds poorly to the diverged Mu TIRs of inactive elements. Previous studies have reported a correlation between Mu transposon inactivation and methylation of the Mu element TIRs. Gel mobility shift assays demonstrate that MURA can interact differentially with unmethylated, hemimethylated, and homomethylated TIR substrates. The significance of MURA's interaction with the TIRs of Mu elements is discussed in the context of what is known about the regulation and mechanisms of Mutator activities in maize.

Resistance to Alfalfa mosaic virus in transgenic barrel medic lines containing the virus coat protein gene

2001 ◽  
Vol 52 (1) ◽  
pp. 67 ◽  
Author(s):  
K. W. Jayasena ◽  
M. R. Hajimorad ◽  
E. G. Law ◽  
A-U. Rehman ◽  
K. E. Nolan ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Medicago Truncatula ◽  
Coat Protein Gene ◽  
Protein Gene ◽  
Single Gene ◽  
Alfalfa Mosaic Virus ◽  
Systemic Infection ◽  
Gene Copy ◽  
Sense Orientation

Medicago truncatula is used as a pasture legume and a source of nitrogen for grain crops in southern Australia. Alfalfa mosaic virus (AMV) infection reduces herbage production and nodulation. The coat protein gene of a South Australian strain of AMV (AMV N20) has been transferred to Medicago truncatula cv. Jemalong 2HA using Agrobacterium-mediated transformation. The most detailed investigations were carried out with the coat protein gene in the sense orientation (CP+). Progeny (T1, T2, T3) raised from self-pollinated primary transformants (T0) containing the coat protein CP+ gene were resistant to AMV. Based on Southern analysis and segregation, the transformants contained a single gene copy. In the T3 generation, one line was immune and one line showed resistance to AMV N20. The immune line contained no detectable virus when plant sap from either inoculated or systemic leaves was bioassayed on Phaseolus vulgaris. This line was also immune to the heterologous AMV S40 isolate. A line with the coat protein gene in antisense orientation (CP–) showed delayed systemic infection but was not immune. We conclude that coat protein mediated protection (CPMP) is an effective strategy for controlling AMV infection and should be further evaluated in the field.

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